SCAF_ELHVK
ID SCAF_ELHVK Reviewed; 564 AA.
AC Q18LE3;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Capsid scaffolding protein {ECO:0000255|HAMAP-Rule:MF_04008};
DE AltName: Full=Protease precursor {ECO:0000255|HAMAP-Rule:MF_04008};
DE Short=pPR {ECO:0000255|HAMAP-Rule:MF_04008};
DE Contains:
DE RecName: Full=Assemblin {ECO:0000255|HAMAP-Rule:MF_04008};
DE EC=3.4.21.97 {ECO:0000255|HAMAP-Rule:MF_04008};
DE AltName: Full=Protease {ECO:0000255|HAMAP-Rule:MF_04008};
DE Contains:
DE RecName: Full=Assembly protein {ECO:0000255|HAMAP-Rule:MF_04008};
DE AltName: Full=Capsid assembly protein {ECO:0000255|HAMAP-Rule:MF_04008};
OS Elephantid herpesvirus 1 (isolate Asian elephant/Berlin/Kiba/1998) (EIHV-1)
OS (Elephant endotheliotropic herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Proboscivirus.
OX NCBI_TaxID=654902;
OH NCBI_TaxID=9783; Elephas maximus (Indian elephant).
OH NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH NCBI_TaxID=99490; Loxodonta cyclotis (African forest elephant).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17507487; DOI=10.1128/jvi.00255-07;
RA Ehlers B., Kuchler J., Yasmum N., Dural G., Voigt S., Schmidt-Chanasit J.,
RA Jakel T., Matuschka F.R., Richter D., Essbauer S., Hughes D.J., Summers C.,
RA Bennett M., Stewart J.P., Ulrich R.G.;
RT "Identification of novel rodent herpesviruses, including the first
RT gammaherpesvirus of Mus musculus.";
RL J. Virol. 81:8091-8100(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11172087; DOI=10.1099/0022-1317-82-3-475;
RA Ehlers B., Burkhardt S., Goltz M., Bergmann V., Ochs A., Weiler H.,
RA Hentschke J.;
RT "Genetic and ultrastructural characterization of a European isolate of the
RT fatal endotheliotropic elephant herpesvirus.";
RL J. Gen. Virol. 82:475-482(2001).
CC -!- FUNCTION: [Capsid scaffolding protein]: Acts as a scaffold protein by
CC binding major capsid protein in the cytoplasm, inducing the nuclear
CC localization of both proteins. Multimerizes in the nucleus such as
CC major capsid protein forms the icosahedral T=16 capsid. Autocatalytic
CC cleavage releases the assembly protein, and subsequently abolishes
CC interaction with major capsid protein. Cleavages products are evicted
CC from the capsid before or during DNA packaging. {ECO:0000255|HAMAP-
CC Rule:MF_04008}.
CC -!- FUNCTION: [Assemblin]: Protease that plays an essential role in virion
CC assembly within the nucleus. Catalyzes the cleavage of the assembly
CC protein after formation of the spherical procapsid. By that cleavage,
CC the capsid matures and gains its icosahedral shape. The cleavage sites
CC seem to include -Ala-Ser-, -Ala-Ala-, as well as Ala-Thr bonds.
CC Assemblin and cleavages products are evicted from the capsid before or
CC during DNA packaging. {ECO:0000255|HAMAP-Rule:MF_04008}.
CC -!- FUNCTION: [Assembly protein]: Plays a major role in capsid assembly.
CC Acts as a scaffold protein by binding major capsid protein.
CC Multimerizes in the nucleus such as major capsid protein forms the
CC icosahedral T=16 capsid. Cleaved by assemblin after capsid completion.
CC The cleavages products are evicted from the capsid before or during DNA
CC packaging. {ECO:0000255|HAMAP-Rule:MF_04008}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold
CC protein.; EC=3.4.21.97; Evidence={ECO:0000255|HAMAP-Rule:MF_04008};
CC -!- SUBUNIT: Capsid scaffolding protein homomultimerizes and interacts with
CC major capsid protein. Assemblin exists in a monomer-dimer equilibrium
CC with the dimer being the active species. Assembly protein
CC homomultimerizes and interacts with major capsid protein.
CC {ECO:0000255|HAMAP-Rule:MF_04008}.
CC -!- SUBCELLULAR LOCATION: [Capsid scaffolding protein]: Host cytoplasm
CC {ECO:0000255|HAMAP-Rule:MF_04008}.
CC -!- SUBCELLULAR LOCATION: [Assemblin]: Host nucleus {ECO:0000255|HAMAP-
CC Rule:MF_04008}.
CC -!- SUBCELLULAR LOCATION: [Assembly protein]: Host nucleus
CC {ECO:0000255|HAMAP-Rule:MF_04008}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=Capsid scaffolding protein; Synonyms=pPR;
CC IsoId=Q18LE3-1; Sequence=Displayed;
CC Name=pAP; Synonyms=Assembly protein;
CC IsoId=Q18LE3-2; Sequence=VSP_041023;
CC -!- DOMAIN: Region of interaction between pPR and pAP is called Amino
CC conserved domain (ACD). The region of interaction with major capsid
CC protein is called carboxyl conserved domain (CCD). {ECO:0000255|HAMAP-
CC Rule:MF_04008}.
CC -!- PTM: Capsid scaffolding protein is cleaved by assemblin after formation
CC of the spherical procapsid. As a result, the capsid obtains its mature,
CC icosahedral shape. Cleavages occur at two or more sites: release and
CC tail site. {ECO:0000255|HAMAP-Rule:MF_04008}.
CC -!- SIMILARITY: Belongs to the herpesviridae capsid scaffolding protein
CC family. {ECO:0000255|HAMAP-Rule:MF_04008}.
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DR EMBL; AF322977; ABG36576.1; -; Genomic_DNA.
DR SMR; Q18LE3; -.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.16.10; -; 1.
DR HAMAP; MF_04008; HSV_SCAF; 1.
DR InterPro; IPR035443; Herpes_virus_sf.
DR InterPro; IPR001847; Peptidase_S21.
DR Pfam; PF00716; Peptidase_S21; 1.
DR PRINTS; PR00236; HSVCAPSIDP40.
PE 3: Inferred from homology;
KW Alternative promoter usage; Host cytoplasm; Host nucleus; Hydrolase;
KW Phosphoprotein; Protease; Serine protease; Viral capsid assembly;
KW Viral release from host cell.
FT CHAIN 1..564
FT /note="Capsid scaffolding protein"
FT /id="PRO_0000408158"
FT CHAIN 1..272
FT /note="Assemblin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000408159"
FT CHAIN 273..564
FT /note="Assembly protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000408160"
FT REGION 306..325
FT /note="Interaction with pAP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT REGION 544..564
FT /note="Interaction with major capsid protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 91
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 176
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT SITE 272..273
FT /note="Cleavage; by assemblin; Release site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT VAR_SEQ 1..299
FT /note="Missing (in isoform pAP)"
FT /evidence="ECO:0000305"
FT /id="VSP_041023"
SQ SEQUENCE 564 AA; 63107 MW; 6C3BAA3A3FE1CAB5 CRC64;
MCIILSSSNF IDPSDDLVNI FSVICIIRCL KSFCMVRWAP TLDMSSRVFF GGFVVVHDAD
TDETLVIDKD VVDYVFSNNL DGENTPLNIN HREDAVVGNV FKFFSVDRGI FCIGEITSKR
FLKIIKNASN DSCVVGLGPT APVPKDSILE YLSAYLPALS LSNFVSPSET RPFFRHVSLC
GLGRRRGTLV AYGRSIPWII SKFKCLSKRD VKRILNFKIP GPVSPFNQET FLLDPEFLLA
TSTDITCIDR RKNTLSYDKK LACLDNESYV RASANCPNCL YYSHSEENKE GLVKTVSINM
NKFPDSEGVY LSKEAFLGLL KQTAYRGLPG CYGMYDHPIA QPHICYQPHG ILAAAQAFDN
DELVLQPASK RRRIEYLPLP GEQQHEKHTS QQKHGSAILQ QHQPQVQSIQ PISTMAVDST
SGDHTINAIK EMCTALVDIR KDLDILKRKS EENTQKYSHF QPHVPNQQDN LLTTRAIIHQ
APESAANNQA QQQHSIADNV TNQTAHPSVQ QASLAANVQH QSEVVNAGHT FTKNQTHQHN
NQPRDDILNH NKKLFIAALS SSDH
